The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition
One of the most common lesions present in the spermatozoa of human infertility patients is an idiopathic failure of sperm-egg recognition. Although this unique cellular interaction can now be readily by-passed by assisted reproductive strategies such as intracytoplasmic sperm injection (ICSI), recen...
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doaj-56079126922f4ef6a3e11160dfe751db2020-11-25T00:45:28ZengWolters Kluwer Medknow PublicationsAsian Journal of Andrology1008-682X1745-72622015-01-0117456857310.4103/1008-682X.151395The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognitionBrett NixonElizabeth G BromfieldMatthew D DunKate A RedgroveEileen A McLaughlinR John AitkenOne of the most common lesions present in the spermatozoa of human infertility patients is an idiopathic failure of sperm-egg recognition. Although this unique cellular interaction can now be readily by-passed by assisted reproductive strategies such as intracytoplasmic sperm injection (ICSI), recent large-scale epidemiological studies have encouraged the cautious use of this technology and highlighted the need for further research into the mechanisms responsible for defective sperm-egg recognition. Previous work in this field has established that the sperm domains responsible for oocyte interaction are formed during spermatogenesis prior to being dynamically modified during epididymal maturation and capacitation in female reproductive tract. While the factors responsible for the regulation of these sequential maturational events are undoubtedly complex, emerging research has identified the molecular chaperone, heat shock protein A2 (HSPA2), as a key regulator of these events in human spermatozoa. HSPA2 is a testis-enriched member of the 70 kDa heat shock protein family that promotes the folding, transport, and assembly of protein complexes and has been positively correlated with in vitro fertilization (IVF) success. Furthermore, reduced expression of HSPA2 from the human sperm proteome leads to an impaired capacity for cumulus matrix dispersal, sperm-egg recognition and fertilization following both IVF and ICSI. In this review, we consider the evidence supporting the role of HSPA2 in sperm function and explore the potential mechanisms by which it is depleted in the spermatozoa of infertile patients. Such information offers novel insights into the molecular mechanisms governing sperm function.http://www.ajandrology.com/article.asp?issn=1008-682X;year=2015;volume=17;issue=4;spage=568;epage=573;aulast=Nixongene regulationMusashiMusashi-1Musashi-2posttranscriptional controlRNA binding proteinsspermatogenesissplicingtestistranslationcell fatecell stressimportinkaryopherinnucleocytoplasmic transportspermatidspermatocytespermatogenesisartificial inseminationbiomarkerfertilityfertilizationflow cytometryinfertilitynanotechnologyoocyte activationPostacrosomal Sheath WWI Domain Binding ProteinspermSPTRX3thioredoxinubiquitinATP binding cassette transportersalbuminhigh-density lipoproteinlipid raftsmembrane fluiditymembrane microdomainsmembrane packingoxysterolsreverse cholesterol transportsterol transporterseggfertilizationheat shock protein A2molecular chaperonespermsperm-egg interactions |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Brett Nixon Elizabeth G Bromfield Matthew D Dun Kate A Redgrove Eileen A McLaughlin R John Aitken |
spellingShingle |
Brett Nixon Elizabeth G Bromfield Matthew D Dun Kate A Redgrove Eileen A McLaughlin R John Aitken The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition Asian Journal of Andrology gene regulation Musashi Musashi-1 Musashi-2 posttranscriptional control RNA binding proteins spermatogenesis splicing testis translation cell fate cell stress importin karyopherin nucleocytoplasmic transport spermatid spermatocyte spermatogenesis artificial insemination biomarker fertility fertilization flow cytometry infertility nanotechnology oocyte activation Postacrosomal Sheath WWI Domain Binding Protein sperm SPTRX3 thioredoxin ubiquitin ATP binding cassette transporters albumin high-density lipoprotein lipid rafts membrane fluidity membrane microdomains membrane packing oxysterols reverse cholesterol transport sterol transporters egg fertilization heat shock protein A2 molecular chaperone sperm sperm-egg interactions |
author_facet |
Brett Nixon Elizabeth G Bromfield Matthew D Dun Kate A Redgrove Eileen A McLaughlin R John Aitken |
author_sort |
Brett Nixon |
title |
The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition |
title_short |
The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition |
title_full |
The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition |
title_fullStr |
The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition |
title_full_unstemmed |
The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition |
title_sort |
role of the molecular chaperone heat shock protein a2 (hspa2) in regulating human sperm-egg recognition |
publisher |
Wolters Kluwer Medknow Publications |
series |
Asian Journal of Andrology |
issn |
1008-682X 1745-7262 |
publishDate |
2015-01-01 |
description |
One of the most common lesions present in the spermatozoa of human infertility patients is an idiopathic failure of sperm-egg recognition. Although this unique cellular interaction can now be readily by-passed by assisted reproductive strategies such as intracytoplasmic sperm injection (ICSI), recent large-scale epidemiological studies have encouraged the cautious use of this technology and highlighted the need for further research into the mechanisms responsible for defective sperm-egg recognition. Previous work in this field has established that the sperm domains responsible for oocyte interaction are formed during spermatogenesis prior to being dynamically modified during epididymal maturation and capacitation in female reproductive tract. While the factors responsible for the regulation of these sequential maturational events are undoubtedly complex, emerging research has identified the molecular chaperone, heat shock protein A2 (HSPA2), as a key regulator of these events in human spermatozoa. HSPA2 is a testis-enriched member of the 70 kDa heat shock protein family that promotes the folding, transport, and assembly of protein complexes and has been positively correlated with in vitro fertilization (IVF) success. Furthermore, reduced expression of HSPA2 from the human sperm proteome leads to an impaired capacity for cumulus matrix dispersal, sperm-egg recognition and fertilization following both IVF and ICSI. In this review, we consider the evidence supporting the role of HSPA2 in sperm function and explore the potential mechanisms by which it is depleted in the spermatozoa of infertile patients. Such information offers novel insights into the molecular mechanisms governing sperm function. |
topic |
gene regulation Musashi Musashi-1 Musashi-2 posttranscriptional control RNA binding proteins spermatogenesis splicing testis translation cell fate cell stress importin karyopherin nucleocytoplasmic transport spermatid spermatocyte spermatogenesis artificial insemination biomarker fertility fertilization flow cytometry infertility nanotechnology oocyte activation Postacrosomal Sheath WWI Domain Binding Protein sperm SPTRX3 thioredoxin ubiquitin ATP binding cassette transporters albumin high-density lipoprotein lipid rafts membrane fluidity membrane microdomains membrane packing oxysterols reverse cholesterol transport sterol transporters egg fertilization heat shock protein A2 molecular chaperone sperm sperm-egg interactions |
url |
http://www.ajandrology.com/article.asp?issn=1008-682X;year=2015;volume=17;issue=4;spage=568;epage=573;aulast=Nixon |
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